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Biochem Lecture 5
Review of Protein Structure
| Question | Answer |
|---|---|
| Amino acids are joined by amide linkages called _______ forming linear chains called ______. | peptide bonds; polypeptides |
| The _________ group is covalently attached to the _________ group of the next amino acid. | a-Carboxyl group; a-Amino group |
| What is the byproduct of a peptide bond? | H20 |
| Are peptide bonds broken when proteins get denatured? | No! |
| Peptide bonds are in the ______ configuration. | TRANS |
| A ______ residue causes limited flexibility due to it's nitrogen being incorporated into the Pyrrolidine ring | Proline |
| The carboxyl (-C=O) and amino (-NH) groups of thepeptide bond are polar and involved in _______ bonds. | Hydrogen |
| The ending of the name of each amino acid in a chain is changed to ____ except the one at the C-terminus | "yl" |
| The Linear Sequence of Amino Acids linked by peptide bonds that determines 3-D structure and the function of the protein. | Primary structure |
| Localized structures within proteins that are formed from hydrogen bonds between -C=O and -NH of the peptide bond. | Secondary structure |
| In ________ H-bonds are formed between the carbonyl oxygen of a peptide bond and the hydrogen attached to the amide group of a peptide bond that is 4 amino acids away | Alpha Helices |
| In _______ H-bonds are formed between linear regions of the polypeptide | Beta Sheets |
| What are the 2 comformations of Beta Sheets? | Parallel and Anti-parallel |
| What 2 amino acids are often involved in a B turn of a Beta Sheet? | Proline and Glycine |
| _______ make up 50% of most polypeptide chains | Loop/Coil |
| What three super secondary structures are often found in DNA binding proteins? | Helix-turn-helix, Zinc finger, Leucine zipper |
| The 3-D conformation of a protein | Tertiary structure |
| ______ interactions are the most important in the folding of the peptide chain. | Hydrophobic |
| Apart from Hydrophobic interactions, what other interactions help to form the tertiary structure of a protein? | Hydrogen bonds, ionic bonds (electrostatic interactions), and S-S (disulfide bonds) |
| What is a domain? | Independent folding region that allows 1 protein to have multiple functions. Each domain has a specific function. |
| Found in proteins that have multiple subunits (multiple polypeptide chains) | Quaternary structure |
| Multiple subunits are held together by _________. | noncovalent interactions and/or disulfide bonds |
| _________ aid in protein folding during synthesis. They also prevent misfolding and protein aggregation | Chaperones |
| _____ is required for chaperones to fold proteins. | ATP |
| What structures do denatured proteins lose? | Secondary, Tertiary, quaternary |
| What can cause denaturization of proteins? | pH extremes, temperature, Ionic detergents, Organic solvents, Heavy Metal Ions, and Mechanical Stress. |
Created by:
chilangberto
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